Proteases are major components of rattlesnake venom, which are used for self-defense and prey immobilization.  Different proteases act on either soluble or insoluble substrates.  The proteases in rattlesnake venom have been found to be extremely heat stable, exhibiting activity at 70<sup>o</sup>C.  This study investigates which intramolecular forces are important in the protein structure and, therefore, the heat stability of these enzymes.  Reagents known to disrupt specific intramolecular forces were used sequentially, and their effects on the activity of the protease at varying temperatures were documented.  This was done for proteases acting on both soluble and insoluble substrates.  The effects due to the disruption of hydrogen bonding, salt bridges, hydrophobic interactions, and disulfides bonds were investigated.  The results provide insight into which intramolecular forces are critical for the proteases’ extreme heat stability.

Role of intramolecular forces in protease heat stability

251st National Meeting (2016)

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